{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T19:40:08Z","timestamp":1768506008227,"version":"3.49.0"},"posted":{"date-parts":[[2023,4,20]]},"group-title":"Microbiology","reference-count":44,"publisher":"openRxiv","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2023,4,20]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                <jats:p>\n                  <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                  is an opportunistic pathogen that can establish acute and chronic infections in individuals that lack fully functional innate immunity. In particular, phagocytosis by neutrophils and macrophages is a key mechanism that modulates host control and clearance of\n                  <jats:italic>P. aeruginosa<\/jats:italic>\n                  . Individuals with neutropenia or cystic fibrosis are highly susceptible to\n                  <jats:italic>P. aeruginosa<\/jats:italic>\n                  infection thus underscoring the importance of the host innate immune response. Cell-to-cell contact between host innate immune cells and the pathogen, a first step in phagocytic uptake, is facilitated by simple and complex glycan structures present at the host cell surface. We have previously shown that endogenous polyanionic N-linked glycans localized to the cell surface of phagocytes mediate binding and subsequent phagocytosis of\n                  <jats:italic>P. aeruginosa<\/jats:italic>\n                  . However, the suite of glycans that\n                  <jats:italic>P. aeruginosa<\/jats:italic>\n                  binds to on host phagocytic cells remains poorly characterized. Here we demonstrate, with the use of exogenous N-linked glycans and a glycan array, that\n                  <jats:italic>P. aeruginosa<\/jats:italic>\n                  PAO1 preferentially attaches to a subset of glycans, including a bias towards monosaccharide versus more complex glycan structures. Consistent with these findings, we were able to competitively inhibit bacterial adherence and uptake by the addition of exogenous N-linked mono- and di-saccharide glycans. We discuss of findings in the context of previous reports of\n                  <jats:italic>P. aeruginosa<\/jats:italic>\n                  glycan binding.\n                <\/jats:p>\n                <jats:sec>\n                  <jats:title>IMPORTANCE<\/jats:title>\n                  <jats:p>\n                    <jats:italic>P. aeruginosa<\/jats:italic>\n                    binds to a variety of glycans as part of its interaction with host cells, and a number of\n                    <jats:italic>P. aeruginosa-<\/jats:italic>\n                    encoded receptors and target ligands have been described that allow this microbe to bind to such glycans. Here we extend this work by studying the glycans used by\n                    <jats:italic>P. aeruginosa<\/jats:italic>\n                    PAO1 to bind to phagocytic cells and by using a glycan array to characterize the suite of such molecules that could facilitate host cell-binding by this microbe. This study provides an increased understanding of the glycans bound by\n                    <jats:italic>P. aeruginosa<\/jats:italic>\n                    , and furthermore, provides a useful dataset for future studies of\n                    <jats:italic>P. aeruginosa-<\/jats:italic>\n                    glycan interactions.\n                  <\/jats:p>\n                <\/jats:sec>","DOI":"10.1101\/2023.04.20.537720","type":"posted-content","created":{"date-parts":[[2023,4,21]],"date-time":"2023-04-21T01:20:10Z","timestamp":1682040010000},"source":"Crossref","is-referenced-by-count":0,"title":["Assessment of the Glycan-Binding Profile of\n                  <i>Pseudomonas aeruginosa<\/i>\n                  PAO1"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1982-2453","authenticated-orcid":false,"given":"Hector","family":"Sanchez","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2861-4392","authenticated-orcid":false,"given":"George A.","family":"O\u2019Toole","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9196-3256","authenticated-orcid":false,"given":"Brent","family":"Berwin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"54368","reference":[{"key":"2023042503401231000_2023.04.20.537720v1.1","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00036-10"},{"key":"2023042503401231000_2023.04.20.537720v1.2","doi-asserted-by":"publisher","DOI":"10.1016\/S1286-4579(00)01259-4"},{"key":"2023042503401231000_2023.04.20.537720v1.3","doi-asserted-by":"publisher","DOI":"10.1016\/S1286-4579(00)01259-4"},{"key":"2023042503401231000_2023.04.20.537720v1.4","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00144-10"},{"key":"2023042503401231000_2023.04.20.537720v1.5","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002253"},{"key":"2023042503401231000_2023.04.20.537720v1.6","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.16.4.597-621.2003"},{"key":"2023042503401231000_2023.04.20.537720v1.7","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00501-09"},{"key":"2023042503401231000_2023.04.20.537720v1.8","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2006.02.015"},{"key":"2023042503401231000_2023.04.20.537720v1.9","first-page":"e00215","article-title":"Phosphatidylinositol-(3,4,5)-Trisphosphate 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